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Rockefeller University Press, Journal of Cell Biology, 2(199), p. 381-399, 2012

DOI: 10.1083/jcb.201202012

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Localization of Usher 1 proteins to the photoreceptor calyceal processes, which are absent from mice.

Journal article published in 2012 by Iman Sahly, Eric Dufour, Cataldo Schietroma, Vincent Michel, Amel Bahloul ORCID, Isabelle Perfettini, Elise Pepermans, Amrit Estivalet, Diane Carette, Asadollah Aghaie ORCID, Inga Ebermann, Andrea Lelli, Maria Iribarne, Jean-Pierre Hardelin, Dominique Weil and other authors.
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The mechanisms underlying retinal dystrophy in Usher syndrome type I (USH1) remain unknown because mutant mice lacking any of the USH1 proteins-myosin VIIa, harmonin, cadherin-23, protocadherin-15, sans-do not display retinal degeneration. We found here that, in macaque photoreceptor cells, all USH1 proteins colocalized at membrane interfaces (i) between the inner and outer segments in rods and (ii) between the microvillus-like calyceal processes and the outer segment basolateral region in rods and cones. This pattern, conserved in humans and frogs, was mediated by the formation of an USH1 protein network, which was associated with the calyceal processes from the early embryonic stages of outer segment growth onwards. By contrast, mouse photoreceptors lacked calyceal processes and had no USH1 proteins at the inner-outer segment interface. We suggest that USH1 proteins form an adhesion belt around the basolateral region of the photoreceptor outer segment in humans, and that defects in this structure cause the retinal degeneration in USH1 patients.